. Author manuscript; available in PMC: 2016 Jan 22.

Published in final edited form as: Cell Rep. 2015 Nov 12;13(8):1683–1691. doi: 10.1016/j.celrep.2015.10.027

Table 1.

Glycan-binding properties of wild-type and mutant dkEgy10 and ckViet08 H5 HAs^*

	130-loop insertion	220-loop	158-glycosylation	LSTa	LSTc
dkEgy10 (E5.0)	–	K224, Q226	D158, A160	+++++	−
E5.1	–	K224, *L226*	D158, A160	−	++++
E5.2	*S133a*	K224, *L226*	D158, A160	−	−
E5.3	–	K224, *L226*	*N158, T160*	+	−
E5.4	*S133a*	K224, Q226	D158, A160	+	−
E5.5	*S133a*	K224, *L226*	*N158, T160*	−	−
E5.6	–	K224, Q226	*N158, T160*	−	−

ckViet08 (V4.4)	–	*K224, L226*	*D158*, T160	+	++++

Viet04 mutant	L133a	*K224, L226*	*D158*, T160	−	−

Ind05 mutant	S133a	*L226, S228*	N158, *A160*	−	−

The key RBS residues in H5 HAs for switch of receptor specificity are shown for wild-type dkEgy10 HA (E5.0) and its mutants. The mutated residues from wild-type HA are highlighted in bold italics. Apparent receptor binding on a glycan binding assay: +++++ very strong; ++++ strong; + weak/variable; − not detected. Viet04 mutant is the HA of ferret-transmissible A/Viet Nam/1203/2004 (with HA mutants N158D, N224K, Q226L and T318I) (Imai et al., 2012) and Ind05 mutant is the HA of ferret-transmissible A/Indonesia/5/2005 (with mutations H110Y, T160A, Q226L and G228S) (Herfst et al., 2012).